ID Q87LT7_VIBPA Unreviewed; 561 AA.
AC Q87LT7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Type IV pilin assembly protein PilB {ECO:0000313|EMBL:BAC60787.1};
GN OrderedLocusNames=VP2524 {ECO:0000313|EMBL:BAC60787.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC60787.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC60787.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
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DR EMBL; BA000031; BAC60787.1; -; Genomic_DNA.
DR RefSeq; NP_798903.1; NC_004603.1.
DR RefSeq; WP_005479695.1; NC_004603.1.
DR AlphaFoldDB; Q87LT7; -.
DR GeneID; 1190039; -.
DR KEGG; vpa:VP2524; -.
DR PATRIC; fig|223926.6.peg.2421; -.
DR eggNOG; COG2804; Bacteria.
DR HOGENOM; CLU_013446_10_1_6; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0009297; P:pilus assembly; IEA:InterPro.
DR CDD; cd01129; PulE-GspE-like; 1.
DR Gene3D; 3.30.450.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR013374; ATPase_typ4_pilus-assembl_PilB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR007831; T2SS_GspE_N.
DR NCBIfam; TIGR02538; type_IV_pilB; 1.
DR PANTHER; PTHR30258:SF1; PROTEIN TRANSPORT PROTEIN HOFB HOMOLOG; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00437; T2SSE; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493}.
FT DOMAIN 383..397
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 561 AA; 62392 MW; 9603891B43FF04B0 CRC64;
MHSNLSTILR QKGLLTFSQE ESLIEQVKAS GISMPEALLS SGFFTSSELA EHLSSIFGLS
QPELSQYEYA SLCQQLGLRE LITRHNALPL HRTPSTLLLA VADPTNQQAE DDFRFATGLQ
VELVLADFRE LSTAIRRLYG RSLSHEKSGL KEINQEELAS LVDVGADEID NIEDLSQDES
PVSRYINQIL LDAVRKGASD IHFEPYEKMY RVRLRCDGIL IETQQPPNHL SRRLSARIKI
LSKLDIAERR LPQDGRIKLK LNQDTAIDMR VSTLPTLFGE KIVLRLLDSS SASLDIDKLG
YSEQQKQLYL EALRRPQGMI LMTGPTGSGK TVSLYTGLNI LNKPEINIST AEDPVEINLS
GINQVQVQPK IGFGFAEALR SFLRQDPDVV MVGEIRDLDT AEIAIKASQT GHLVLSTLHT
NSAAETIIRL SNMGVESFNL ASSLSLIIAQ RLARKLCPYC KQPQEHTVQL QHLGIQTTDN
IFRANPDGCN ECTHGYSGRT GIYEVMRFDE SLSEALIKGA SVHELEKLAI ANGMSTLQMS
GIEKLKQGIT SFSELQRVLY F
//
